Partial dehydration of high-salt horse methaemoglobin crystals tends to shift the structure from the R state to the R2 state, in agreement with previous observations that movements in the molecule resulting from changes in water content mimic those involved in protein action.

T. brucei gene Tb10.6k15.0140 codes for an α/β-hydrolase fold protein of unknown function. The 2.2 Å crystal structure shows that members of this sequence family retain a conserved Ser residue at the expected site of a catalytic nucleophile, but that trypanosomatid sequences lack structural homologs for the other expected residues of the catalytic triad.

Three conventional robots were subjected to a crystallization screening test involving 18 proteins from T. thermophilus HB8 using the sitting- and hanging-drop vapour-diffusion and microbatch methods. The number of diffraction-quality crystals and the amount of time required to obtain visible crystals depended greatly on the robots used. The combined use of different robots, especially for protein samples exhibiting low crystallization success rates, significantly increased the chance of obtaining diffraction-quality crystals.

CMS1MS2, a cysteine proteinase from C. candamarcensis, displays high amidase activity against the substrate BAPNA. The enzyme was purified and crystallized by the hanging-drop method and preliminary diffraction data were collected to 1.8 Å resolution.

Mcm10 is a highly conserved nuclear protein that plays a key role in the initiation and elongation processes of DNA replication by providing a physical link between the Mcm2–7 complex and DNA polymerases. In this study, the central domain of human Mcm10 was crystallized using the hanging-drop vapour-diffusion method in the presence of PEG 3350.

NCDV VP8*64–224 was expressed in E. coli, purified and crystallized in the presence of a sialic acid derivative. X-ray diffraction data were obtained to a resolution of 2.0 Å and the crystallographic structure was determined by molecular replacement.

CapF, a capsular polysaccharide-assembling protein from S. aureus, has been crystallized using the hanging-drop vapour-diffusion method. Oprimization of the crystallization conditions by differential scanning calorimetry afforded a crystal of selenomethionine-substituted CapF that diffracted to a resolution of 2.80 Å.

Human prouroguanylin, a precursor protein of a peptide hormone, was expressed in E. coli, refolded, purified and crystallized. The crystals belong to space group P6122 and diffract X-rays to 2.5 Å resolution.

The crystallization and preliminary neutron crystallographic analysis of selectively CH3-protonated deuterated rubredoxin from P. furiosus is presented. This work represents the first reported use of selectively labeled material for phasing applications using neutron protein crystallography.

The production and purification of recombinant SoGST3 and SoGST6, two GST-like proteins from S. oneidensis, are reported and preliminary crystallographic studies of crystals of the recombinant enzymes are presented.

The cloning, overexpression, purification, crystallization and preliminary X-ray diffraction analysis of H. pylori MotB, a peptidoglycan-binding component of the stator of the bacterial flagellar motor, are reported.